Matrix metalloproteinase-7 degrades all insulin-like growth factor binding proteins and facilitates insulin-like growth factor bioavailability
作者： Michio Nakamura , Shin’ichi Miyamoto , Hiroyuki Maeda , Genichiro Ishii , Takahiro Hasebe
DOI: 10.1016/J.BBRC.2005.06.010
关键词:
摘要: Proteolytic modification of insulin-like growth factor binding proteins (IGFBPs) plays an important physiological role in regulating (IGF) bioavailability. Recently, we demonstrated that matrix metalloproteinase-7 (MMP-7)/Matrilysin produced by various cancer cells catalyzes the proteolysis IGFBP-3 vitro and regulates IGF bioavailability, resulting anti-apoptotic effect against anchorage-independent culture. In present study, investigated whether MMP-7 contributes to other five IGFBPs, IGFBP-1, IGFBP-2, IGFBP-4, IGFBP-5, IGFBP-6, this results phosphorylation type 1 receptor (IGF-1R). cleaved all six IGF-mediated IGF-1R phosphorylation, which was inhibited EDTA treatment. These suggest derived from can regulate bioavailability microenvironment surrounding tumor, where kinds IGF/IGFBP complexes are found, thereby favoring cell survival during processes invasion metastasis.
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